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Binding properties of the human homeodomain protein OTX2 to a DNA target sequence
Author(s) -
Briata Paola,
Ilengo Cristina,
Bobola Nicoletta,
Corte Giorgio
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00113-1
Subject(s) - homeobox , dna , binding site , dna binding site , dna binding protein , dna footprinting , microbiology and biotechnology , biology , plasma protein binding , recombinant dna , genetics , gene , chemistry , promoter , transcription factor , gene expression
OTX2, a homeodomain protein essential in mouse for the development of structures anterior to rhombomere 3, binds with high affinity to a DNA element (called OTS) present in the human tenascin‐C promoter. Here we investigate the binding properties of the full length recombinant human OTX2 and of several deletion mutants to the OTS element. We demonstrate that, upon binding of the protein to its DNA target site, a second molecule of OTX2 is recruited to the complex and that a nearby second binding site is not necessary for this interaction. OTX2 sequences located within a region carboxyl‐terminal to the homeodomain are necessary in addition to the homeodomain for binding to DNA. Furthermore, OTX2 dimerization requires the same protein domains necessary for DNA binding.